Figure 5.
Figure 5. The inner surface of the TPR superhelix features a
ladder of asparagines. (a) Schematic of the inside face of
the superhelix, showing residues present at positions 6 (top
row) and 9 (bottom row) in the TPR repeats. Absolutely conserved
asparagines (Fig. 3a) are highlighted in red. TPR repeats 13 and
14, shaded in gray, are not present in the crystal structure.
(b) Stereo view of electron density around the conserved
asparagines of TPR repeats 3 and 4 in chain 2 with the final
model superimposed. The 2.85-Å electron density map is contoured
at 1.1 .
(c) Ribbon drawing of TPR repeats 2 -4 (helices A in yellow,
helices B in gray) with solvent-exposed residues highlighted.
The position in the TPR consensus sequence (Fig. 3a) of each
residue is indicated with circled numbers.
The above figure is reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Mol Biol
(2004,
11,
1001-1007)
copyright 2004.
.
(c) Ribbon drawing of TPR repeats 2 -4 (helices A in yellow,
helices B in gray) with solvent-exposed residues highlighted.
The position in the TPR consensus sequence (Fig. 3a) of each
residue is indicated with circled numbers.